Pub Date : 2016-01-01DOI: 10.1007/978-3-319-21756-7_5
F. Crea, C. De Stefano, C. Foti, G. Lando, D. Milea, S. Sammartano
{"title":"Alkali Metal Ion Complexes with Phosphates, Nucleotides, Amino Acids, and Related Ligands of Biological Relevance. Their Properties in Solution.","authors":"F. Crea, C. De Stefano, C. Foti, G. Lando, D. Milea, S. Sammartano","doi":"10.1007/978-3-319-21756-7_5","DOIUrl":"https://doi.org/10.1007/978-3-319-21756-7_5","url":null,"abstract":"","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"7 1","pages":"133-66"},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74235740","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-01-01DOI: 10.1007/978-3-319-21756-7_6
P. Auffinger, Luigi D’Ascenzo, E. Ennifar
{"title":"Sodium and Potassium Interactions with Nucleic Acids.","authors":"P. Auffinger, Luigi D’Ascenzo, E. Ennifar","doi":"10.1007/978-3-319-21756-7_6","DOIUrl":"https://doi.org/10.1007/978-3-319-21756-7_6","url":null,"abstract":"","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"7 1","pages":"167-201"},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88005247","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-01-01DOI: 10.1007/978-3-319-21756-7_3
K. Aoki, K. Murayama, N. Hu
{"title":"Solid State Structures of Alkali Metal Ion Complexes Formed by Low-Molecular-Weight Ligands of Biological Relevance.","authors":"K. Aoki, K. Murayama, N. Hu","doi":"10.1007/978-3-319-21756-7_3","DOIUrl":"https://doi.org/10.1007/978-3-319-21756-7_3","url":null,"abstract":"","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"8 4 1","pages":"27-101"},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78356258","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-01-01DOI: 10.1007/978-3-319-21756-7_14
Nuria Rodríguez-Vázquez, A. Fuertes, M. Amorín, J. Granja
{"title":"Bioinspired Artificial Sodium and Potassium Ion Channels.","authors":"Nuria Rodríguez-Vázquez, A. Fuertes, M. Amorín, J. Granja","doi":"10.1007/978-3-319-21756-7_14","DOIUrl":"https://doi.org/10.1007/978-3-319-21756-7_14","url":null,"abstract":"","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"12 1","pages":"485-556"},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77007240","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-01-01DOI: 10.1007/978-3-319-21756-7_11
G. Fritz, J. Steuber
{"title":"Sodium as Coupling Cation in Respiratory Energy Conversion.","authors":"G. Fritz, J. Steuber","doi":"10.1007/978-3-319-21756-7_11","DOIUrl":"https://doi.org/10.1007/978-3-319-21756-7_11","url":null,"abstract":"","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"25 1","pages":"349-90"},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89106060","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-01-01DOI: 10.1007/978-3-319-21756-7_9
M. Nieves‐Cordones, Fouad Razzaq A Al Shiblawi, H. Sentenac
{"title":"Roles and Transport of Sodium and Potassium in Plants.","authors":"M. Nieves‐Cordones, Fouad Razzaq A Al Shiblawi, H. Sentenac","doi":"10.1007/978-3-319-21756-7_9","DOIUrl":"https://doi.org/10.1007/978-3-319-21756-7_9","url":null,"abstract":"","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"1 1","pages":"291-324"},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76008490","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-01-01DOI: 10.1007/978-3-319-21756-7_1
Youngsam Kim, T. Nguyen, D. Churchill
{"title":"Bioinorganic Chemistry of the Alkali Metal Ions.","authors":"Youngsam Kim, T. Nguyen, D. Churchill","doi":"10.1007/978-3-319-21756-7_1","DOIUrl":"https://doi.org/10.1007/978-3-319-21756-7_1","url":null,"abstract":"","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"7 1","pages":"1-10"},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80855308","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2015-01-01DOI: 10.1007/978-3-319-12415-5_3
Jennifer L DuBois, Sunil Ojha
O₂-generating reactions are exceedingly rare in biology and difficult to mimic synthetically. Perchlorate-respiring bacteria enzymatically detoxify chlorite (ClO₂(-) ), the end product of the perchlorate (ClO(4)(-) ) respiratory pathway, by rapidly converting it to dioxygen (O₂) and chloride (Cl(-)). This reaction is catalyzed by a heme-containing protein, called chlorite dismutase (Cld), which bears no structural or sequence relationships with known peroxidases or other heme proteins and is part of a large family of proteins with more than one biochemical function. The original assumptions from the 1990s that perchlorate is not a natural product and that perchlorate respiration might be confined to a taxonomically narrow group of species have been called into question, as have the roles of perchlorate respiration and Cld-mediated reactions in the global biogeochemical cycle of chlorine. In this chapter, the chemistry and biochemistry of Cld-mediated O₂generation, as well as the biological and geochemical context of this extraordinary reaction, are described.
{"title":"Production of dioxygen in the dark: dismutases of oxyanions.","authors":"Jennifer L DuBois, Sunil Ojha","doi":"10.1007/978-3-319-12415-5_3","DOIUrl":"10.1007/978-3-319-12415-5_3","url":null,"abstract":"<p><p>O₂-generating reactions are exceedingly rare in biology and difficult to mimic synthetically. Perchlorate-respiring bacteria enzymatically detoxify chlorite (ClO₂(-) ), the end product of the perchlorate (ClO(4)(-) ) respiratory pathway, by rapidly converting it to dioxygen (O₂) and chloride (Cl(-)). This reaction is catalyzed by a heme-containing protein, called chlorite dismutase (Cld), which bears no structural or sequence relationships with known peroxidases or other heme proteins and is part of a large family of proteins with more than one biochemical function. The original assumptions from the 1990s that perchlorate is not a natural product and that perchlorate respiration might be confined to a taxonomically narrow group of species have been called into question, as have the roles of perchlorate respiration and Cld-mediated reactions in the global biogeochemical cycle of chlorine. In this chapter, the chemistry and biochemistry of Cld-mediated O₂generation, as well as the biological and geochemical context of this extraordinary reaction, are described.</p>","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"15 ","pages":"45-87"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-3-319-12415-5_3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33076955","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2015-01-01DOI: 10.1007/978-3-319-12415-5_7
Joachim Reimann, Mike S M Jetten, Jan T Keltjens
Ammonium and methane are inert molecules and dedicated enzymes are required to break up the N-H and C-H bonds. Until recently, only aerobic microorganisms were known to grow by the oxidation of ammonium or methane. Apart from respiration, oxygen was specifically utilized to activate the inert substrates. The presumed obligatory need for oxygen may have resisted the search for microorganisms that are capable of the anaerobic oxidation of ammonium and of methane. However extremely slowly growing, these "impossible" organisms exist and they found other means to tackle ammonium and methane. Anaerobic ammonium-oxidizing (anammox) bacteria use the oxidative power of nitric oxide (NO) by forging this molecule to ammonium, thereby making hydrazine (N2H4). Nitrite-dependent anaerobic methane oxidizers (N-DAMO) again take advantage of NO, but now apparently disproportionating the compound into dinitrogen and dioxygen gas. This intracellularly produced dioxygen enables N-DAMO bacteria to adopt an aerobic mechanism for methane oxidation.Although our understanding is only emerging how hydrazine synthase and the NO dismutase act, it seems clear that reactions fully rely on metal-based catalyses known from other enzymes. Metal-dependent conversions not only hold for these key enzymes, but for most other reactions in the central catabolic pathways, again supported by well-studied enzymes from model organisms, but adapted to own specific needs. Remarkably, those accessory catabolic enzymes are not unique for anammox bacteria and N-DAMO. Close homologs are found in protein databases where those homologs derive from (partly) known, but in most cases unknown species that together comprise an only poorly comprehended microbial world.
{"title":"Metal enzymes in \"impossible\" microorganisms catalyzing the anaerobic oxidation of ammonium and methane.","authors":"Joachim Reimann, Mike S M Jetten, Jan T Keltjens","doi":"10.1007/978-3-319-12415-5_7","DOIUrl":"https://doi.org/10.1007/978-3-319-12415-5_7","url":null,"abstract":"<p><p>Ammonium and methane are inert molecules and dedicated enzymes are required to break up the N-H and C-H bonds. Until recently, only aerobic microorganisms were known to grow by the oxidation of ammonium or methane. Apart from respiration, oxygen was specifically utilized to activate the inert substrates. The presumed obligatory need for oxygen may have resisted the search for microorganisms that are capable of the anaerobic oxidation of ammonium and of methane. However extremely slowly growing, these \"impossible\" organisms exist and they found other means to tackle ammonium and methane. Anaerobic ammonium-oxidizing (anammox) bacteria use the oxidative power of nitric oxide (NO) by forging this molecule to ammonium, thereby making hydrazine (N2H4). Nitrite-dependent anaerobic methane oxidizers (N-DAMO) again take advantage of NO, but now apparently disproportionating the compound into dinitrogen and dioxygen gas. This intracellularly produced dioxygen enables N-DAMO bacteria to adopt an aerobic mechanism for methane oxidation.Although our understanding is only emerging how hydrazine synthase and the NO dismutase act, it seems clear that reactions fully rely on metal-based catalyses known from other enzymes. Metal-dependent conversions not only hold for these key enzymes, but for most other reactions in the central catabolic pathways, again supported by well-studied enzymes from model organisms, but adapted to own specific needs. Remarkably, those accessory catabolic enzymes are not unique for anammox bacteria and N-DAMO. Close homologs are found in protein databases where those homologs derive from (partly) known, but in most cases unknown species that together comprise an only poorly comprehended microbial world. </p>","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"15 ","pages":"257-313"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-3-319-12415-5_7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33076958","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2015-01-01DOI: 10.1007/978-3-319-12415-5
P. Kroneck, Martha E Sosa Torres
{"title":"Sustaining Life on Planet Earth: Metalloenzymes Mastering Dioxygen and Other Chewy Gases","authors":"P. Kroneck, Martha E Sosa Torres","doi":"10.1007/978-3-319-12415-5","DOIUrl":"https://doi.org/10.1007/978-3-319-12415-5","url":null,"abstract":"","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"79 1","pages":"vii-ix"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82409168","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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